CA3117275A1 - Stabilized pre-fusion rsv f proteins - Google Patents
Stabilized pre-fusion rsv f proteins Download PDFInfo
- Publication number
- CA3117275A1 CA3117275A1 CA3117275A CA3117275A CA3117275A1 CA 3117275 A1 CA3117275 A1 CA 3117275A1 CA 3117275 A CA3117275 A CA 3117275A CA 3117275 A CA3117275 A CA 3117275A CA 3117275 A1 CA3117275 A1 CA 3117275A1
- Authority
- CA
- Canada
- Prior art keywords
- fusion
- amino acid
- protein
- rsv
- mutation
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Pending
Links
- 230000004927 fusion Effects 0.000 title claims abstract description 179
- 108090000623 proteins and genes Proteins 0.000 title claims abstract description 77
- 102000004169 proteins and genes Human genes 0.000 title claims abstract description 76
- 241000725643 Respiratory syncytial virus Species 0.000 claims abstract description 203
- 108010068327 4-hydroxyphenylpyruvate dioxygenase Proteins 0.000 claims abstract description 199
- 239000000203 mixture Substances 0.000 claims abstract description 27
- 206010061603 Respiratory syncytial virus infection Diseases 0.000 claims abstract description 11
- 238000011282 treatment Methods 0.000 claims abstract description 6
- 230000035772 mutation Effects 0.000 claims description 190
- 125000000539 amino acid group Chemical group 0.000 claims description 101
- 229940024606 amino acid Drugs 0.000 claims description 100
- 150000001413 amino acids Chemical class 0.000 claims description 99
- 230000000087 stabilizing effect Effects 0.000 claims description 56
- 150000007523 nucleic acids Chemical class 0.000 claims description 53
- 108020004707 nucleic acids Proteins 0.000 claims description 51
- 102000039446 nucleic acids Human genes 0.000 claims description 51
- 239000013598 vector Substances 0.000 claims description 38
- 229960005486 vaccine Drugs 0.000 claims description 21
- 230000028993 immune response Effects 0.000 claims description 15
- 238000005829 trimerization reaction Methods 0.000 claims description 14
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 claims description 10
- 229930182817 methionine Natural products 0.000 claims description 10
- 230000001939 inductive effect Effects 0.000 claims description 8
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 claims description 7
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 claims description 7
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 claims description 7
- 229960000310 isoleucine Drugs 0.000 claims description 7
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 claims description 5
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 claims description 5
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 claims description 4
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 claims description 4
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 claims description 4
- 239000004472 Lysine Substances 0.000 claims description 4
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 claims description 4
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 claims description 4
- 239000004473 Threonine Substances 0.000 claims description 4
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 claims description 4
- 239000004474 valine Substances 0.000 claims description 4
- 210000004962 mammalian cell Anatomy 0.000 claims description 3
- 238000011321 prophylaxis Methods 0.000 claims description 3
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 claims description 2
- 230000002163 immunogen Effects 0.000 abstract description 4
- 230000002265 prevention Effects 0.000 abstract description 4
- 235000001014 amino acid Nutrition 0.000 description 86
- 235000018102 proteins Nutrition 0.000 description 68
- 238000000034 method Methods 0.000 description 39
- 210000004027 cell Anatomy 0.000 description 32
- 125000003275 alpha amino acid group Chemical group 0.000 description 18
- 239000012634 fragment Substances 0.000 description 16
- 230000007935 neutral effect Effects 0.000 description 16
- 108020004705 Codon Proteins 0.000 description 15
- 238000003860 storage Methods 0.000 description 12
- 239000002671 adjuvant Substances 0.000 description 8
- 201000010099 disease Diseases 0.000 description 8
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 8
- 108010076504 Protein Sorting Signals Proteins 0.000 description 7
- 239000012528 membrane Substances 0.000 description 7
- 230000003472 neutralizing effect Effects 0.000 description 7
- 238000006467 substitution reaction Methods 0.000 description 7
- 241000700605 Viruses Species 0.000 description 6
- 230000027455 binding Effects 0.000 description 6
- 208000015181 infectious disease Diseases 0.000 description 6
- 238000002844 melting Methods 0.000 description 6
- 230000008018 melting Effects 0.000 description 6
- 239000000546 pharmaceutical excipient Substances 0.000 description 6
- 108090000765 processed proteins & peptides Proteins 0.000 description 6
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 5
- 210000004899 c-terminal region Anatomy 0.000 description 5
- 238000005516 engineering process Methods 0.000 description 5
- 108020001507 fusion proteins Proteins 0.000 description 5
- 102000037865 fusion proteins Human genes 0.000 description 5
- 238000000746 purification Methods 0.000 description 5
- 239000000243 solution Substances 0.000 description 5
- 239000006228 supernatant Substances 0.000 description 5
- 108091035707 Consensus sequence Proteins 0.000 description 4
- 238000002965 ELISA Methods 0.000 description 4
- 101710189104 Fibritin Proteins 0.000 description 4
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 4
- 108700019146 Transgenes Proteins 0.000 description 4
- 238000004458 analytical method Methods 0.000 description 4
- 244000052769 pathogen Species 0.000 description 4
- 230000001717 pathogenic effect Effects 0.000 description 4
- 239000008194 pharmaceutical composition Substances 0.000 description 4
- 239000002243 precursor Substances 0.000 description 4
- 102000004196 processed proteins & peptides Human genes 0.000 description 4
- 230000003612 virological effect Effects 0.000 description 4
- 108010011170 Ala-Trp-Arg-His-Pro-Gln-Phe-Gly-Gly Proteins 0.000 description 3
- 241000282412 Homo Species 0.000 description 3
- 108091028043 Nucleic acid sequence Proteins 0.000 description 3
- 102000035195 Peptidases Human genes 0.000 description 3
- 108091005804 Peptidases Proteins 0.000 description 3
- 239000004365 Protease Substances 0.000 description 3
- 206010057190 Respiratory tract infections Diseases 0.000 description 3
- 239000000427 antigen Substances 0.000 description 3
- 230000000890 antigenic effect Effects 0.000 description 3
- 108091007433 antigens Proteins 0.000 description 3
- 102000036639 antigens Human genes 0.000 description 3
- 238000013459 approach Methods 0.000 description 3
- 238000003556 assay Methods 0.000 description 3
- 238000012258 culturing Methods 0.000 description 3
- 230000001086 cytosolic effect Effects 0.000 description 3
- 238000002022 differential scanning fluorescence spectroscopy Methods 0.000 description 3
- 210000003527 eukaryotic cell Anatomy 0.000 description 3
- 239000000499 gel Substances 0.000 description 3
- 238000003306 harvesting Methods 0.000 description 3
- 210000005260 human cell Anatomy 0.000 description 3
- 229940035032 monophosphoryl lipid a Drugs 0.000 description 3
- 229920001184 polypeptide Polymers 0.000 description 3
- 238000002360 preparation method Methods 0.000 description 3
- 239000000523 sample Substances 0.000 description 3
- 230000006641 stabilisation Effects 0.000 description 3
- 238000011105 stabilization Methods 0.000 description 3
- 208000024891 symptom Diseases 0.000 description 3
- 238000012360 testing method Methods 0.000 description 3
- 238000002255 vaccination Methods 0.000 description 3
- 210000002845 virion Anatomy 0.000 description 3
- 239000011534 wash buffer Substances 0.000 description 3
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 2
- 208000034628 Celiac artery compression syndrome Diseases 0.000 description 2
- 108700010070 Codon Usage Proteins 0.000 description 2
- 108020004414 DNA Proteins 0.000 description 2
- 230000006820 DNA synthesis Effects 0.000 description 2
- 102000004961 Furin Human genes 0.000 description 2
- 108090001126 Furin Proteins 0.000 description 2
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 2
- 239000004471 Glycine Substances 0.000 description 2
- 102000003886 Glycoproteins Human genes 0.000 description 2
- 108090000288 Glycoproteins Proteins 0.000 description 2
- 108091092195 Intron Proteins 0.000 description 2
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 2
- 238000011529 RT qPCR Methods 0.000 description 2
- 239000002253 acid Substances 0.000 description 2
- XAGFODPZIPBFFR-UHFFFAOYSA-N aluminium Chemical compound [Al] XAGFODPZIPBFFR-UHFFFAOYSA-N 0.000 description 2
- 229910052782 aluminium Inorganic materials 0.000 description 2
- 239000004411 aluminium Substances 0.000 description 2
- WNROFYMDJYEPJX-UHFFFAOYSA-K aluminium hydroxide Chemical compound [OH-].[OH-].[OH-].[Al+3] WNROFYMDJYEPJX-UHFFFAOYSA-K 0.000 description 2
- 229910021502 aluminium hydroxide Inorganic materials 0.000 description 2
- ILRRQNADMUWWFW-UHFFFAOYSA-K aluminium phosphate Chemical compound O1[Al]2OP1(=O)O2 ILRRQNADMUWWFW-UHFFFAOYSA-K 0.000 description 2
- 229940001007 aluminium phosphate Drugs 0.000 description 2
- 229910000147 aluminium phosphate Inorganic materials 0.000 description 2
- 230000003097 anti-respiratory effect Effects 0.000 description 2
- 239000011324 bead Substances 0.000 description 2
- 229940098773 bovine serum albumin Drugs 0.000 description 2
- 238000004113 cell culture Methods 0.000 description 2
- 230000001413 cellular effect Effects 0.000 description 2
- 230000008859 change Effects 0.000 description 2
- 238000003776 cleavage reaction Methods 0.000 description 2
- 238000010276 construction Methods 0.000 description 2
- 239000012228 culture supernatant Substances 0.000 description 2
- 235000018417 cysteine Nutrition 0.000 description 2
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 2
- 210000005220 cytoplasmic tail Anatomy 0.000 description 2
- 238000012217 deletion Methods 0.000 description 2
- 230000037430 deletion Effects 0.000 description 2
- 238000001514 detection method Methods 0.000 description 2
- 239000003814 drug Substances 0.000 description 2
- 239000003937 drug carrier Substances 0.000 description 2
- 239000000975 dye Substances 0.000 description 2
- 239000000839 emulsion Substances 0.000 description 2
- 239000003623 enhancer Substances 0.000 description 2
- -1 enhancer(s) Chemical class 0.000 description 2
- 239000013604 expression vector Substances 0.000 description 2
- 239000007850 fluorescent dye Substances 0.000 description 2
- 239000001963 growth medium Substances 0.000 description 2
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 2
- 230000002209 hydrophobic effect Effects 0.000 description 2
- 230000036039 immunity Effects 0.000 description 2
- 238000000338 in vitro Methods 0.000 description 2
- 238000011534 incubation Methods 0.000 description 2
- 230000002401 inhibitory effect Effects 0.000 description 2
- 239000002502 liposome Substances 0.000 description 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 238000005259 measurement Methods 0.000 description 2
- 239000002609 medium Substances 0.000 description 2
- 238000001823 molecular biology technique Methods 0.000 description 2
- 238000000569 multi-angle light scattering Methods 0.000 description 2
- 239000002105 nanoparticle Substances 0.000 description 2
- 239000002773 nucleotide Substances 0.000 description 2
- 125000003729 nucleotide group Chemical group 0.000 description 2
- 230000008488 polyadenylation Effects 0.000 description 2
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 2
- 230000001681 protective effect Effects 0.000 description 2
- 230000002829 reductive effect Effects 0.000 description 2
- 230000001105 regulatory effect Effects 0.000 description 2
- 230000010076 replication Effects 0.000 description 2
- 230000007017 scission Effects 0.000 description 2
- 210000002966 serum Anatomy 0.000 description 2
- 230000009870 specific binding Effects 0.000 description 2
- 238000010561 standard procedure Methods 0.000 description 2
- 239000008174 sterile solution Substances 0.000 description 2
- 238000004114 suspension culture Methods 0.000 description 2
- 238000013518 transcription Methods 0.000 description 2
- 230000035897 transcription Effects 0.000 description 2
- 239000013638 trimer Substances 0.000 description 2
- 108010087967 type I signal peptidase Proteins 0.000 description 2
- OVKKNJPJQKTXIT-JLNKQSITSA-N (5Z,8Z,11Z,14Z,17Z)-icosapentaenoylethanolamine Chemical compound CC\C=C/C\C=C/C\C=C/C\C=C/C\C=C/CCCC(=O)NCCO OVKKNJPJQKTXIT-JLNKQSITSA-N 0.000 description 1
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 1
- 108010088751 Albumins Proteins 0.000 description 1
- 102000009027 Albumins Human genes 0.000 description 1
- 238000012815 AlphaLISA Methods 0.000 description 1
- 241000710929 Alphavirus Species 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
- 231100000699 Bacterial toxin Toxicity 0.000 description 1
- 206010006448 Bronchiolitis Diseases 0.000 description 1
- 108091006060 C-tagged proteins Proteins 0.000 description 1
- 125000001433 C-terminal amino-acid group Chemical group 0.000 description 1
- 102000009016 Cholera Toxin Human genes 0.000 description 1
- 108010049048 Cholera Toxin Proteins 0.000 description 1
- 241000699802 Cricetulus griseus Species 0.000 description 1
- 101710146739 Enterotoxin Proteins 0.000 description 1
- 241000233866 Fungi Species 0.000 description 1
- 108700007698 Genetic Terminator Regions Proteins 0.000 description 1
- 102100039619 Granulocyte colony-stimulating factor Human genes 0.000 description 1
- 102100039620 Granulocyte-macrophage colony-stimulating factor Human genes 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 101000746367 Homo sapiens Granulocyte colony-stimulating factor Proteins 0.000 description 1
- 101000746373 Homo sapiens Granulocyte-macrophage colony-stimulating factor Proteins 0.000 description 1
- 101000914484 Homo sapiens T-lymphocyte activation antigen CD80 Proteins 0.000 description 1
- 108700002232 Immediate-Early Genes Proteins 0.000 description 1
- 206010061598 Immunodeficiency Diseases 0.000 description 1
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 1
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 1
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 1
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 1
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 1
- 206010024971 Lower respiratory tract infections Diseases 0.000 description 1
- 239000007993 MOPS buffer Substances 0.000 description 1
- 241000124008 Mammalia Species 0.000 description 1
- 108010052285 Membrane Proteins Proteins 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 1
- 102220534335 OX-2 membrane glycoprotein_V76G_mutation Human genes 0.000 description 1
- 108091034117 Oligonucleotide Proteins 0.000 description 1
- 206010035664 Pneumonia Diseases 0.000 description 1
- 241000711904 Pneumoviridae Species 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
- 208000018569 Respiratory Tract disease Diseases 0.000 description 1
- 241000283984 Rodentia Species 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- 241000144290 Sigmodon hispidus Species 0.000 description 1
- 239000012505 Superdex™ Substances 0.000 description 1
- 102100027222 T-lymphocyte activation antigen CD80 Human genes 0.000 description 1
- 108010028230 Trp-Ser- His-Pro-Gln-Phe-Glu-Lys Proteins 0.000 description 1
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 1
- 206010046306 Upper respiratory tract infection Diseases 0.000 description 1
- 241000700618 Vaccinia virus Species 0.000 description 1
- 241000251539 Vertebrata <Metazoa> Species 0.000 description 1
- 206010058874 Viraemia Diseases 0.000 description 1
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 1
- 239000004480 active ingredient Substances 0.000 description 1
- 230000001154 acute effect Effects 0.000 description 1
- 238000004115 adherent culture Methods 0.000 description 1
- 235000004279 alanine Nutrition 0.000 description 1
- 159000000013 aluminium salts Chemical class 0.000 description 1
- NTGGOTYRTOXKMQ-UHFFFAOYSA-K aluminum;potassium;phosphate Chemical compound [Al+3].[K+].[O-]P([O-])([O-])=O NTGGOTYRTOXKMQ-UHFFFAOYSA-K 0.000 description 1
- 238000004873 anchoring Methods 0.000 description 1
- 210000004102 animal cell Anatomy 0.000 description 1
- 238000005349 anion exchange Methods 0.000 description 1
- 230000000840 anti-viral effect Effects 0.000 description 1
- 239000003443 antiviral agent Substances 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 235000009582 asparagine Nutrition 0.000 description 1
- 229960001230 asparagine Drugs 0.000 description 1
- 235000003704 aspartic acid Nutrition 0.000 description 1
- 239000012131 assay buffer Substances 0.000 description 1
- 230000000712 assembly Effects 0.000 description 1
- 238000000429 assembly Methods 0.000 description 1
- 101150036080 at gene Proteins 0.000 description 1
- 230000002238 attenuated effect Effects 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 239000000688 bacterial toxin Substances 0.000 description 1
- 238000010923 batch production Methods 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 1
- 239000012472 biological sample Substances 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 108010006025 bovine growth hormone Proteins 0.000 description 1
- 239000000872 buffer Substances 0.000 description 1
- 238000005341 cation exchange Methods 0.000 description 1
- 239000006143 cell culture medium Substances 0.000 description 1
- 210000000170 cell membrane Anatomy 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 229940001442 combination vaccine Drugs 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 230000021615 conjugation Effects 0.000 description 1
- 238000010924 continuous production Methods 0.000 description 1
- NKLPQNGYXWVELD-UHFFFAOYSA-M coomassie brilliant blue Chemical compound [Na+].C1=CC(OCC)=CC=C1NC1=CC=C(C(=C2C=CC(C=C2)=[N+](CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=2C=CC(=CC=2)N(CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=C1 NKLPQNGYXWVELD-UHFFFAOYSA-M 0.000 description 1
- 239000013078 crystal Substances 0.000 description 1
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 1
- 230000034994 death Effects 0.000 description 1
- 231100000517 death Toxicity 0.000 description 1
- 230000005860 defense response to virus Effects 0.000 description 1
- 239000003599 detergent Substances 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 238000002405 diagnostic procedure Methods 0.000 description 1
- 239000003085 diluting agent Substances 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 238000005538 encapsulation Methods 0.000 description 1
- 210000002472 endoplasmic reticulum Anatomy 0.000 description 1
- 239000000147 enterotoxin Substances 0.000 description 1
- 231100000655 enterotoxin Toxicity 0.000 description 1
- 238000005558 fluorometry Methods 0.000 description 1
- 238000009472 formulation Methods 0.000 description 1
- 239000012537 formulation buffer Substances 0.000 description 1
- 238000012395 formulation development Methods 0.000 description 1
- 125000000524 functional group Chemical group 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- 230000009931 harmful effect Effects 0.000 description 1
- 210000000987 immune system Anatomy 0.000 description 1
- 230000003053 immunization Effects 0.000 description 1
- 238000002649 immunization Methods 0.000 description 1
- 229960001438 immunostimulant agent Drugs 0.000 description 1
- 230000003308 immunostimulating effect Effects 0.000 description 1
- 238000000126 in silico method Methods 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 239000012678 infectious agent Substances 0.000 description 1
- 206010022000 influenza Diseases 0.000 description 1
- 208000037797 influenza A Diseases 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 238000007918 intramuscular administration Methods 0.000 description 1
- 238000010255 intramuscular injection Methods 0.000 description 1
- 239000007927 intramuscular injection Substances 0.000 description 1
- 230000002427 irreversible effect Effects 0.000 description 1
- 229910052743 krypton Inorganic materials 0.000 description 1
- DNNSSWSSYDEUBZ-UHFFFAOYSA-N krypton atom Chemical compound [Kr] DNNSSWSSYDEUBZ-UHFFFAOYSA-N 0.000 description 1
- 239000003446 ligand Substances 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 229920002521 macromolecule Polymers 0.000 description 1
- 230000008774 maternal effect Effects 0.000 description 1
- 230000035800 maturation Effects 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 229960001521 motavizumab Drugs 0.000 description 1
- 230000004719 natural immunity Effects 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- 239000007764 o/w emulsion Substances 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 238000005457 optimization Methods 0.000 description 1
- 210000001672 ovary Anatomy 0.000 description 1
- 238000007911 parenteral administration Methods 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 230000037361 pathway Effects 0.000 description 1
- 230000010412 perfusion Effects 0.000 description 1
- 229940124531 pharmaceutical excipient Drugs 0.000 description 1
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 108091033319 polynucleotide Proteins 0.000 description 1
- 102000040430 polynucleotide Human genes 0.000 description 1
- 239000002157 polynucleotide Substances 0.000 description 1
- 229920000136 polysorbate Polymers 0.000 description 1
- 230000002028 premature Effects 0.000 description 1
- 230000037452 priming Effects 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 210000001236 prokaryotic cell Anatomy 0.000 description 1
- 230000000069 prophylactic effect Effects 0.000 description 1
- 235000019419 proteases Nutrition 0.000 description 1
- 230000006916 protein interaction Effects 0.000 description 1
- 230000030788 protein refolding Effects 0.000 description 1
- 229940023143 protein vaccine Drugs 0.000 description 1
- 239000001397 quillaja saponaria molina bark Substances 0.000 description 1
- 230000008707 rearrangement Effects 0.000 description 1
- 102000005962 receptors Human genes 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 210000002345 respiratory system Anatomy 0.000 description 1
- 208000020029 respiratory tract infectious disease Diseases 0.000 description 1
- 230000001177 retroviral effect Effects 0.000 description 1
- 102220320732 rs1554306350 Human genes 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 229930182490 saponin Natural products 0.000 description 1
- 150000007949 saponins Chemical class 0.000 description 1
- 238000013341 scale-up Methods 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 238000002864 sequence alignment Methods 0.000 description 1
- 238000002741 site-directed mutagenesis Methods 0.000 description 1
- 238000001542 size-exclusion chromatography Methods 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 239000003381 stabilizer Substances 0.000 description 1
- 238000011146 sterile filtration Methods 0.000 description 1
- 230000000638 stimulation Effects 0.000 description 1
- 238000007920 subcutaneous administration Methods 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 229940031626 subunit vaccine Drugs 0.000 description 1
- 230000001225 therapeutic effect Effects 0.000 description 1
- 230000036962 time dependent Effects 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 238000004448 titration Methods 0.000 description 1
- 230000009466 transformation Effects 0.000 description 1
- 230000009261 transgenic effect Effects 0.000 description 1
- 210000004881 tumor cell Anatomy 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- 241001529453 unidentified herpesvirus Species 0.000 description 1
- 239000000277 virosome Substances 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/005—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from viruses
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/12—Viral antigens
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/12—Antivirals
- A61P31/14—Antivirals for RNA viruses
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/70—Fusion polypeptide containing domain for protein-protein interaction
- C07K2319/735—Fusion polypeptide containing domain for protein-protein interaction containing a domain for self-assembly, e.g. a viral coat protein (includes phage display)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N2760/00—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA ssRNA viruses negative-sense
- C12N2760/00011—Details
- C12N2760/18011—Paramyxoviridae
- C12N2760/18511—Pneumovirus, e.g. human respiratory syncytial virus
- C12N2760/18522—New viral proteins or individual genes, new structural or functional aspects of known viral proteins or genes
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N2760/00—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA ssRNA viruses negative-sense
- C12N2760/00011—Details
- C12N2760/18011—Paramyxoviridae
- C12N2760/18511—Pneumovirus, e.g. human respiratory syncytial virus
- C12N2760/18534—Use of virus or viral component as vaccine, e.g. live-attenuated or inactivated virus, VLP, viral protein
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Virology (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Pharmacology & Pharmacy (AREA)
- Molecular Biology (AREA)
- Microbiology (AREA)
- Immunology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Mycology (AREA)
- Genetics & Genomics (AREA)
- Epidemiology (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Gastroenterology & Hepatology (AREA)
- Communicable Diseases (AREA)
- Oncology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP18205863 | 2018-11-13 | ||
| EP18205863.6 | 2018-11-13 | ||
| PCT/EP2019/080989 WO2020099383A1 (en) | 2018-11-13 | 2019-11-12 | Stabilized pre-fusion rsv f proteins |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA3117275A1 true CA3117275A1 (en) | 2020-05-22 |
Family
ID=64308587
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA3117275A Pending CA3117275A1 (en) | 2018-11-13 | 2019-11-12 | Stabilized pre-fusion rsv f proteins |
Country Status (19)
| Country | Link |
|---|---|
| US (1) | US20220017574A1 (ja) |
| EP (1) | EP3880243A1 (ja) |
| JP (1) | JP2022513025A (ja) |
| KR (1) | KR20210091749A (ja) |
| CN (1) | CN113164583A (ja) |
| AU (1) | AU2019377989A1 (ja) |
| BR (1) | BR112021008975A2 (ja) |
| CA (1) | CA3117275A1 (ja) |
| CL (1) | CL2021001212A1 (ja) |
| CO (1) | CO2021006308A2 (ja) |
| CR (1) | CR20210306A (ja) |
| EA (1) | EA202191355A1 (ja) |
| EC (1) | ECSP21042554A (ja) |
| IL (1) | IL282892A (ja) |
| JO (1) | JOP20210106A1 (ja) |
| MX (1) | MX2021005607A (ja) |
| PE (1) | PE20211469A1 (ja) |
| SG (1) | SG11202104522UA (ja) |
| WO (1) | WO2020099383A1 (ja) |
Families Citing this family (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US10456462B2 (en) | 2015-07-07 | 2019-10-29 | Janssen Vaccines & Preventions B.V. | Vaccine against RSV |
| WO2017174564A1 (en) | 2016-04-05 | 2017-10-12 | Janssen Vaccines & Prevention B.V. | Vaccine against rsv |
| PL3464331T3 (pl) | 2016-05-30 | 2021-04-19 | Janssen Vaccines & Prevention B.V. | Stabilizowane przedfuzyjne białka F RSV |
| JP2024509756A (ja) * | 2021-02-19 | 2024-03-05 | ヤンセン ファッシンズ アンド プリベンション ベーフェー | 安定化された融合前ｒｓｖ ｆｂ抗原 |
| KR20230047033A (ko) * | 2021-09-29 | 2023-04-06 | 에스케이바이오사이언스(주) | 재조합된 약독화 rsv 생백신 및 이를 제조하는 방법 |
| CN115850396B (zh) * | 2022-12-22 | 2024-02-06 | 北京吉诺卫生物科技有限公司 | 一种rsv纳米颗粒疫苗及其制备方法与应用 |
| CN117304280B (zh) * | 2023-11-28 | 2024-04-16 | 江苏瑞科生物技术股份有限公司 | 一种重组rsv f蛋白及其应用 |
| CN117304279B (zh) * | 2023-11-28 | 2024-04-16 | 江苏瑞科生物技术股份有限公司 | 一种重组rsv f蛋白及其应用 |
| CN117777251B (zh) * | 2024-02-27 | 2024-06-04 | 普大生物科技(泰州)有限公司 | 一种rsv纳米颗粒疫苗及其制备方法 |
Family Cites Families (31)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4235877A (en) | 1979-06-27 | 1980-11-25 | Merck & Co., Inc. | Liposome particle containing viral or bacterial antigenic subunit |
| US4372945A (en) | 1979-11-13 | 1983-02-08 | Likhite Vilas V | Antigen compounds |
| IL61904A (en) | 1981-01-13 | 1985-07-31 | Yeda Res & Dev | Synthetic vaccine against influenza virus infections comprising a synthetic peptide and process for producing same |
| EP0173552B1 (en) | 1984-08-24 | 1991-10-09 | The Upjohn Company | Recombinant dna compounds and the expression of polypeptides such as tpa |
| US5168062A (en) | 1985-01-30 | 1992-12-01 | University Of Iowa Research Foundation | Transfer vectors and microorganisms containing human cytomegalovirus immediate-early promoter-regulatory DNA sequence |
| US5057540A (en) | 1987-05-29 | 1991-10-15 | Cambridge Biotech Corporation | Saponin adjuvant |
| NZ230747A (en) | 1988-09-30 | 1992-05-26 | Bror Morein | Immunomodulating matrix comprising a complex of at least one lipid and at least one saponin; certain glycosylated triterpenoid saponins derived from quillaja saponaria molina |
| JPH0832638B2 (ja) | 1989-05-25 | 1996-03-29 | カイロン コーポレイション | サブミクロン油滴乳剤を含んで成るアジュバント製剤 |
| US5786464C1 (en) | 1994-09-19 | 2012-04-24 | Gen Hospital Corp | Overexpression of mammalian and viral proteins |
| AUPM873294A0 (en) | 1994-10-12 | 1994-11-03 | Csl Limited | Saponin preparations and use thereof in iscoms |
| SE0202110D0 (sv) | 2002-07-05 | 2002-07-05 | Isconova Ab | Iscom preparation and use thereof |
| SE0301998D0 (sv) | 2003-07-07 | 2003-07-07 | Isconova Ab | Quil A fraction with low toxicity and use thereof |
| US20100261155A1 (en) * | 2007-06-06 | 2010-10-14 | Nationwide Children's Hospital, Inc. | Methods and compositions relating to viral fusion proteins |
| EP3109258B1 (en) | 2007-12-24 | 2019-01-23 | ID Biomedical Corporation of Quebec | Recombinant rsv antigens |
| DK2445526T3 (en) | 2009-06-24 | 2016-06-27 | Glaxosmithkline Biologicals Sa | Recombinant RSV antigens. |
| EA201270062A1 (ru) | 2009-06-24 | 2013-02-28 | АйДи БАЙОМЕДИКАЛ КОРПОРЕЙШН ОФ КВЕБЕК | Вакцина |
| CA2770737C (en) * | 2009-08-13 | 2020-05-12 | Crucell Holland B.V. | Antibodies against human respiratory syncytial virus (rsv) and methods of use |
| NZ703035A (en) | 2010-07-09 | 2016-06-24 | Crucell Holland Bv | Anti-human respiratory syncytial virus (rsv) antibodies and methods of use |
| CA2835644C (en) | 2011-05-13 | 2021-06-15 | Novartis Ag | Pre-fusion rsv f antigens |
| CN112851766A (zh) * | 2013-03-13 | 2021-05-28 | 美国政府(由卫生和人类服务部的部长所代表) | 融合前rsv f蛋白和其用途 |
| EP2970981B1 (en) * | 2013-03-14 | 2020-10-28 | Emory University | Recombinant rsv with silent mutations, vaccines, and methods related thereto |
| KR102236497B1 (ko) | 2013-04-25 | 2021-04-06 | 얀센 백신스 앤드 프리벤션 비.브이. | 안정화된 가용성 예비융합 ｒｓｖ ｆ 폴리펩타이드 |
| AP2015008893A0 (en) * | 2013-06-17 | 2015-12-31 | Crucell Holland Bv | Stabilized soluble pre-fusion rsv f polypeptides |
| WO2016040556A1 (en) * | 2014-09-12 | 2016-03-17 | Rsv Corporation | Virosomes containing respiratory syncytial virus strain line 19 fusion protein and uses thereof |
| US10456462B2 (en) * | 2015-07-07 | 2019-10-29 | Janssen Vaccines & Preventions B.V. | Vaccine against RSV |
| CN107847581B (zh) * | 2015-07-07 | 2022-03-22 | 扬森疫苗与预防公司 | 稳定化的可溶性融合前rsv f多肽 |
| BR112018008708A2 (pt) * | 2015-10-29 | 2018-11-06 | Univ Emory | rsv quimérico, composições imunogênicas e métodos de uso |
| CN108738312A (zh) * | 2015-12-23 | 2018-11-02 | 辉瑞公司 | Rsv f蛋白突变体 |
| CN115960263A (zh) * | 2016-03-29 | 2023-04-14 | 美国政府(由卫生和人类服务部的部长所代表) | 取代修饰的融合前rsv f蛋白及其用途 |
| PT3439672T (pt) | 2016-04-05 | 2021-02-24 | Janssen Vaccines & Prevention Bv | Proteína f do rsv pré-fusão solúvel e estabilizada para uso na profilaxia de infeção por rsv |
| PL3464331T3 (pl) * | 2016-05-30 | 2021-04-19 | Janssen Vaccines & Prevention B.V. | Stabilizowane przedfuzyjne białka F RSV |
-
2019
- 2019-11-12 CN CN201980074164.XA patent/CN113164583A/zh active Pending
- 2019-11-12 CR CR20210306A patent/CR20210306A/es unknown
- 2019-11-12 AU AU2019377989A patent/AU2019377989A1/en active Pending
- 2019-11-12 EA EA202191355A patent/EA202191355A1/ru unknown
- 2019-11-12 CA CA3117275A patent/CA3117275A1/en active Pending
- 2019-11-12 WO PCT/EP2019/080989 patent/WO2020099383A1/en active Application Filing
- 2019-11-12 EP EP19798149.1A patent/EP3880243A1/en active Pending
- 2019-11-12 JP JP2021525874A patent/JP2022513025A/ja active Pending
- 2019-11-12 PE PE2021000680A patent/PE20211469A1/es unknown
- 2019-11-12 SG SG11202104522UA patent/SG11202104522UA/en unknown
- 2019-11-12 US US17/293,364 patent/US20220017574A1/en active Pending
- 2019-11-12 BR BR112021008975-6A patent/BR112021008975A2/pt unknown
- 2019-11-12 JO JOP/2021/0106A patent/JOP20210106A1/ar unknown
- 2019-11-12 MX MX2021005607A patent/MX2021005607A/es unknown
- 2019-11-12 KR KR1020217017491A patent/KR20210091749A/ko unknown
-
2021
- 2021-05-03 IL IL282892A patent/IL282892A/en unknown
- 2021-05-07 CL CL2021001212A patent/CL2021001212A1/es unknown
- 2021-05-13 CO CONC2021/0006308A patent/CO2021006308A2/es unknown
- 2021-06-11 EC ECSENADI202142554A patent/ECSP21042554A/es unknown
Also Published As
| Publication number | Publication date |
|---|---|
| BR112021008975A2 (pt) | 2021-08-17 |
| EA202191355A1 (ru) | 2021-09-20 |
| AU2019377989A1 (en) | 2023-10-05 |
| CO2021006308A2 (es) | 2021-05-31 |
| CN113164583A (zh) | 2021-07-23 |
| IL282892A (en) | 2021-06-30 |
| JP2022513025A (ja) | 2022-02-07 |
| ECSP21042554A (es) | 2021-11-30 |
| WO2020099383A1 (en) | 2020-05-22 |
| KR20210091749A (ko) | 2021-07-22 |
| EP3880243A1 (en) | 2021-09-22 |
| CL2021001212A1 (es) | 2021-10-22 |
| CR20210306A (es) | 2021-07-22 |
| PE20211469A1 (es) | 2021-08-05 |
| MX2021005607A (es) | 2021-06-30 |
| SG11202104522UA (en) | 2021-05-28 |
| US20220017574A1 (en) | 2022-01-20 |
| JOP20210106A1 (ar) | 2023-01-30 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US11034731B2 (en) | Stabilized soluble pre-fusion RSV F polypeptides | |
| US11759514B2 (en) | Stabilized pre-fusion RSV F proteins | |
| US20220017574A1 (en) | Stabilized pre-fusion rsv f proteins | |
| KR20180027560A (ko) | Rsv에 대한 백신 | |
| WO2017207477A1 (en) | Stabilized pre-fusion rsv f proteins | |
| OA19273A (en) | Stabilized pre-fusion RSV F proteins. |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| EEER | Examination request |
Effective date: 20231106 |
|
| EEER | Examination request |
Effective date: 20231106 |